Abstract
The endoglucanase I (EGI) and the cellobiohydrolase I (CBHI) of the filamentous fungus Trichoderma reesei form a homologous pair of cellulolytic enzymes which nevertheless have different modes of action, We show here that the action of CBHI on bacterial microcrystalline cellulose results in efficient solubilisation but only a slow decrease in its degree of polymerisation. In contrast, the action of EGI results in a rapid decrease of the degree of polymerisation but less efficient overall solubilisation of the substrate. CBHI alone was practically inactive toward cotton which has a high initial degree of polymerisation and a complex morphology. EGI rapidly reduced the degree of polymerisation of cotton, and slowly solubilised part of it Working synergistically, EGI and CBHI solubilised cotton more rapidly and to a greater extent than EGI alone. Our data are consistent with the exoglucanase nature of CBHI and also provide some evidence supporting its processive mode of action.
| Original language | English |
|---|---|
| Pages (from-to) | 885-892 |
| Number of pages | 8 |
| Journal | European Journal of Biochemistry |
| Volume | 251 |
| Issue number | 3 |
| Publication status | Published - 1 Feb 1998 |
| MoE publication type | A1 Journal article-refereed |
Keywords
- cellobiohydrolase
- crystalline cellulose
- endoglucanase
- size-exclusion chromatography
- synergy
- CELLOBIOHYDROLASE-I
- CRYSTALLINE CELLULOSE
- BINDING DOMAIN
- ENZYMATIC-HYDROLYSIS
- CELLULASES
- SYNERGISM
- ADSORPTION
- GENES
- MECHANISM
- FIMI